Abstract. A simple method, based on ethanol fractionation, for the preparation of highly purified human serum albumin with a higher yield than that of the conventional ethanol procedures is described. It consists of two purification steps, namely, precipitation of most of the other plasma proteins from a 3‐fold diluted plasma with ethanol at 42% concentration, pH 5.75 and ‐5°C, leaving over 96% pure albumin in the supernatant, followed by isolectric precipitation of albumin from the supernatant at pH 4.8 and ‐5°C. The paste thus obtained was processed to the final albumin solution according to the conventional methods. The yield of the final albumin with a purity of over 99% was equivalent to 29.5 g/1 of plasma representing a recovery of over 93%. The possibility of recovering other plasma proteins and the suitability for large scale preparation are also discussed. © 1979 Blackwell Publishing Ltd